LDRD_ECOLI
ID LDRD_ECOLI Reviewed; 35 AA.
AC Q6BF25; Q2M7K0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Small toxic polypeptide LdrD;
GN Name=ldrD; OrderedLocusNames=b4453, JW5966;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP IDENTIFICATION, FUNCTION, AND PROBABLE INDUCTION.
RX PubMed=12123448; DOI=10.1046/j.1365-2958.2002.03042.x;
RA Kawano M., Oshima T., Kasai H., Mori H.;
RT "Molecular characterization of long direct repeat (LDR) sequences
RT expressing a stable mRNA encoding for a 35-amino-acid cell-killing peptide
RT and a cis-encoded small antisense RNA in Escherichia coli.";
RL Mol. Microbiol. 45:333-349(2002).
RN [4]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18710431; DOI=10.1111/j.1365-2958.2008.06394.x;
RA Fozo E.M., Kawano M., Fontaine F., Kaya Y., Mendieta K.S., Jones K.L.,
RA Ocampo A., Rudd K.E., Storz G.;
RT "Repression of small toxic protein synthesis by the Sib and OhsC small
RT RNAs.";
RL Mol. Microbiol. 70:1076-1093(2008).
CC -!- FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system.
CC Overexpression causes rapid cell killing and nucleoid condensation of
CC the host cell (PubMed:12123448). Overexpression induces stress-response
CC and a number of membrane protein genes. May inhibit ATP synthesis due
CC to its insertion in the cell inner membrane (By similarity).
CC {ECO:0000250|UniProtKB:P0DPD0, ECO:0000269|PubMed:12123448,
CC ECO:0000269|PubMed:18710431}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression of the proteinaceous toxin is controlled by an
CC antisense sRNA, in this case RdlD. Only a few of these TA systems have
CC been mechanistically characterized; the mechanisms used to control
CC expression of the toxin gene are not necessarily the same (Probable).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Ldr toxic peptide family. {ECO:0000305}.
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DR EMBL; U00096; AAT48189.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77756.1; -; Genomic_DNA.
DR RefSeq; WP_000141634.1; NZ_SSZK01000039.1.
DR RefSeq; YP_026227.1; NC_000913.3.
DR PDB; 5LBJ; NMR; -; A=1-35.
DR PDBsum; 5LBJ; -.
DR AlphaFoldDB; Q6BF25; -.
DR SMR; Q6BF25; -.
DR BioGRID; 4260912; 12.
DR STRING; 511145.b4453; -.
DR TCDB; 1.C.64.1.13; the fst toxin (fst) family.
DR PaxDb; Q6BF25; -.
DR PRIDE; Q6BF25; -.
DR EnsemblBacteria; AAT48189; AAT48189; b4453.
DR EnsemblBacteria; BAE77756; BAE77756; BAE77756.
DR GeneID; 2847730; -.
DR GeneID; 58390103; -.
DR KEGG; ecj:JW5966; -.
DR KEGG; eco:b4453; -.
DR PATRIC; fig|1411691.4.peg.3177; -.
DR HOGENOM; CLU_212598_1_0_6; -.
DR PhylomeDB; Q6BF25; -.
DR BioCyc; EcoCyc:MON0-921; -.
DR PRO; PR:Q6BF25; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008219; P:cell death; IMP:EcoCyc.
DR InterPro; IPR025253; Toxin_Ldr.
DR Pfam; PF13940; Ldr_toxin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Toxin-antitoxin system; Transmembrane;
KW Transmembrane helix.
FT PEPTIDE 1..35
FT /note="Small toxic polypeptide LdrD"
FT /id="PRO_0000230294"
FT TRANSMEM 10..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 3..34
FT /evidence="ECO:0007829|PDB:5LBJ"
SQ SEQUENCE 35 AA; 3917 MW; 25E6A9A8634CD78D CRC64;
MTFAELGMAF WHDLAAPVIA GILASMIVNW LNKRK